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RMLC_METTH
ID   RMLC_METTH              Reviewed;         185 AA.
AC   O27818;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=dTDP-4-dehydrorhamnose 3,5-epimerase {ECO:0000305|PubMed:10827167};
DE            EC=5.1.3.13 {ECO:0000269|PubMed:10827167};
DE   AltName: Full=Thymidine diphospho-4-keto-rhamnose 3,5-epimerase {ECO:0000305|PubMed:10827167};
DE   AltName: Full=dTDP-4-keto-6-deoxyglucose 3,5-epimerase {ECO:0000303|PubMed:10827167};
DE   AltName: Full=dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase {ECO:0000305|PubMed:10827167};
DE   AltName: Full=dTDP-L-rhamnose synthase {ECO:0000305|PubMed:10827167};
GN   Name=rmlC; OrderedLocusNames=MTH_1790;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP   FUNCTION IN DTDP-RHAMNOSE BIOSYNTHESIS, CATALYTIC ACTIVITY, ACTIVE SITE,
RP   AND SUBUNIT.
RX   PubMed=10827167; DOI=10.1074/jbc.c000238200;
RA   Christendat D., Saridakis V., Dharamsi A., Bochkarev A., Pai E.F.,
RA   Arrowsmith C.H., Edwards A.M.;
RT   "Crystal structure of dTDP-4-keto-6-deoxy-D-hexulose 3,5-epimerase from
RT   Methanobacterium thermoautotrophicum complexed with dTDP.";
RL   J. Biol. Chem. 275:24608-24612(2000).
CC   -!- FUNCTION: Catalyzes the epimerization of the C3' and C5'positions of
CC       dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
CC       {ECO:0000269|PubMed:10827167}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-
CC         L-rhamnose; Xref=Rhea:RHEA:16969, ChEBI:CHEBI:57649,
CC         ChEBI:CHEBI:62830; EC=5.1.3.13;
CC         Evidence={ECO:0000269|PubMed:10827167};
CC   -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC       {ECO:0000250|UniProtKB:P26394}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10827167}.
CC   -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000666; AAB86256.1; -; Genomic_DNA.
DR   PIR; B69106; B69106.
DR   RefSeq; WP_010877392.1; NC_000916.1.
DR   PDB; 1EP0; X-ray; 1.50 A; A=1-185.
DR   PDB; 1EPZ; X-ray; 1.75 A; A=1-185.
DR   PDBsum; 1EP0; -.
DR   PDBsum; 1EPZ; -.
DR   AlphaFoldDB; O27818; -.
DR   SMR; O27818; -.
DR   EnsemblBacteria; AAB86256; AAB86256; MTH_1790.
DR   GeneID; 1470875; -.
DR   KEGG; mth:MTH_1790; -.
DR   PATRIC; fig|187420.15.peg.1745; -.
DR   HOGENOM; CLU_090940_1_1_2; -.
DR   OMA; RGVFLEW; -.
DR   UniPathway; UPA00124; -.
DR   EvolutionaryTrace; O27818; -.
DR   Proteomes; UP000005223; Chromosome.
DR   GO; GO:0008830; F:dTDP-4-dehydrorhamnose 3,5-epimerase activity; NAS:UniProtKB.
DR   GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; NAS:UniProtKB.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR000888; dTDP_sugar_isom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR21047; PTHR21047; 1.
DR   Pfam; PF00908; dTDP_sugar_isom; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
DR   TIGRFAMs; TIGR01221; rmlC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Isomerase; Reference proteome.
FT   CHAIN           1..185
FT                   /note="dTDP-4-dehydrorhamnose 3,5-epimerase"
FT                   /id="PRO_0000395351"
FT   ACT_SITE        64
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305|PubMed:10827167"
FT   ACT_SITE        133
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         31
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         49..51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:10827167,
FT                   ECO:0007744|PDB:1EPZ"
FT   BINDING         61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:10827167,
FT                   ECO:0007744|PDB:1EPZ"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   SITE            139
FT                   /note="Participates in a stacking interaction with the
FT                   thymidine ring of dTDP-4-oxo-6-deoxyglucose"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SFD1"
FT   STRAND          4..8
FT                   /evidence="ECO:0007829|PDB:1EP0"
FT   STRAND          15..19
FT                   /evidence="ECO:0007829|PDB:1EP0"
FT   STRAND          21..24
FT                   /evidence="ECO:0007829|PDB:1EP0"
FT   STRAND          27..30
FT                   /evidence="ECO:0007829|PDB:1EP0"
FT   HELIX           35..40
FT                   /evidence="ECO:0007829|PDB:1EP0"
FT   STRAND          49..56
FT                   /evidence="ECO:0007829|PDB:1EP0"
FT   STRAND          59..69
FT                   /evidence="ECO:0007829|PDB:1EP0"
FT   STRAND          73..88
FT                   /evidence="ECO:0007829|PDB:1EP0"
FT   TURN            94..97
FT                   /evidence="ECO:0007829|PDB:1EP0"
FT   STRAND          99..105
FT                   /evidence="ECO:0007829|PDB:1EP0"
FT   TURN            106..108
FT                   /evidence="ECO:0007829|PDB:1EP0"
FT   STRAND          111..114
FT                   /evidence="ECO:0007829|PDB:1EP0"
FT   STRAND          118..124
FT                   /evidence="ECO:0007829|PDB:1EP0"
FT   STRAND          126..137
FT                   /evidence="ECO:0007829|PDB:1EP0"
FT   HELIX           141..143
FT                   /evidence="ECO:0007829|PDB:1EP0"
FT   STRAND          144..146
FT                   /evidence="ECO:0007829|PDB:1EP0"
FT   TURN            152..154
FT                   /evidence="ECO:0007829|PDB:1EP0"
FT   HELIX           160..162
FT                   /evidence="ECO:0007829|PDB:1EP0"
FT   HELIX           170..173
FT                   /evidence="ECO:0007829|PDB:1EP0"
FT   TURN            178..180
FT                   /evidence="ECO:0007829|PDB:1EP0"
SQ   SEQUENCE   185 AA;  21678 MW;  E321B0D881834139 CRC64;
     MAEFRFIKTS LDGAIIIEPE VYTDERGYFM ETFNEAIFQE NGLEVRFVQD NESMSVRGVL
     RGLHFQREKP QGKLVRVIRG EIFDVAVDLR KNSDTYGEWT GVRLSDENRR EFFIPEGFAH
     GFLALSDECI VNYKCTELYH PEYDSGIPWD DPDIGIDWPL EMVDDLIISE KDRNWKPLRE
     NPVYL
 
 
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